5IIH

Crystal structure of Equine Serum Albumin in the presence of 2.5 mM zinc at pH 7.4

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2014-11-26
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.979
Spacegroup name	P 61
Unit cell lengths	93.098, 93.098, 141.442
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.010 - 2.400
R-factor	0.1777
Rwork	0.175
R-free	0.23540
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3v08
RMSD bond length	0.009
RMSD bond angle	1.222
Data reduction software	HKL-3000
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0135)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.010	50.000	2.440
High resolution limit [Å]	2.400	6.510	2.400
Rmerge	0.071	0.032	0.965
Number of reflections	27051
<I/σ(I)>	9.3
Completeness [%]	99.6	98.6	99.3
Redundancy	7.7	7.1	7.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.4	289	1 ul of 30 mg/ml protein in 10 mM Tris pH 7.5 and 150 mM NaCl buffer was mixed with 1 ul of the well condition (0.2 M Li2SO4, 0.1 M Tris:HCl pH 7.4, 2.0 M (NH4)2SO4, 5 mM ZnCl2) and equilibrated against well solution in 15 Well Crystallization Plate (Qiagen)